Edinburgh, Scotland, United Kingdom
- Expert in molecular biology, biochemistry and cell biology - Main interest: proteins involved in various aspects of nucleic acid metabolism - Focus: diseases (including autoimmunity and cancer) caused by perturbation in nucleic acid metabolism
Continuation of my work in the lab of Prof Andrew Jackson, after promotion to Senior Lecturer.
Continuation of my work in the lab of Prof Andrew Jackson, after promotion to Research Fellow.
I work in the lab of Prof Andrew Jackson at the Medical Research Council IGMM, Human Genetics Unit, The University of Edinburgh. Project synopsis: RNase H endonuclease enzymes cleave RNA/DNA hybrids which form during key biological processes. In spite of this, the precise biological roles of these enzymes are poorly understood. RNase H2 is the predominant source of RNase H activity in mammalian cells. It has the apparently unique ability to hydrolyze the 5' phosphodiester bond of single ribonucleotides embedded in a DNA duplex. Mutations in all three subunits of human RNase H2 cause the autoinflammatory disorder AGS, an early-onset progressive encephalopathy with clinical and immunological similarities to congenital viral infections and the common autoimmune disease systemic lupus erythematosus. Inflammation may be triggered by accumulation of nucleic acids generated during DNA replication/repair, or by increased cellular levels of endogenous retroelements. The monogenic nature of AGS provides an important human model to gain insights into nucleic acid-triggered inflammation, and the physiological role of RNase H2 activity. Using biochemistry, molecular biology and cell biology I am investigating the biological functions of RNase H2, with the ultimate aim of dissecting the AGS disease mechanism.
Follow-up of PhD research in the lab of Prof. Jean Beggs at the Wellcome Trust Centre for Cell Biology, The University of Edinburgh.
I worked in the lab of Prof. Jean Beggs at the Wellcome Trust Centre for Cell Biology, The University of Edinburgh Project synopsis: Eukaryotes have two heteroheptameric Lsm protein complexes, nuclear Lsm2-8 and cytoplasmic Lsm1-7. Both have functions in RNA processing. The project aim was to reconstitute Lsm complexes from purified recombinant proteins to examine their function in vitro. In addition, mutational analysis and microscopy were used to study their function and localisation in vivo. From September to December 2004 I taught and supervised Structures & Functions of Proteins (3h), a third-year honours practical course organised by the Edinburgh School of Biology.
I worked in the lab of Dr. Sean Colloms at the Department of Molecular Genetics, University of Glasgow. Project synopsis: E. coli PepA is a bi-functional protein acting both as a peptidase and as a DNA binding protein involved in site-specific recombination. We determined the involvement of specific residues in DNA binding by examining recombination in vitro and in vivo after random or site-directed mutagenesis. This allowed us to build a model showing the way the PepA homohexamer bends DNA necessary for efficient recombination.
I worked under the supervision of Dr. H.M. Schaink & Prof. E. van der Linden at the Department of Food Physics, Wageningen University. In addition to performing research into the heat-induced gelling process of whey proteins, I supervised a practical course in Food Physics to third-year students Food Technology.
I worked in the lab of Prof. Just Vlak under the supervision of Dr. Marielle van Hulten at the Department of Virology, Wageningen University. Project synopsis: White Spot Syndrome Virus (WSSV) is an enveloped, double stranded DNA virus that infects a wide range of crustaceans causing wide-scale economic damage to prawn farming. We used bio-informatics, yeast-2-hybrid analysis and biochemistry to get insight into the interactions between the five WSSV major structural proteins as well as their structure and glycosylation status.